Ontology highlight
ABSTRACT:
SUBMITTER: Lu H
PROVIDER: S-EPMC6680050 | biostudies-literature | 2019 Aug
REPOSITORIES: biostudies-literature
Lu Hui H Xiao Juanjuan J Ke Changshu C Ni Xiaofang X Xiu Ruijuan R Tian Qin Q Pan Huaxiong H Zou Ling L Wang Fei F Ma Tengfei T Ji Xinying X Yuan Ping P Liu Lin L Zhang Jianmin J Jia Wei W Duan Qiuhong Q Zhu Feng F
Cell death & disease 20190805 8
ULK1, the upper-most protein of the ULK1 complex, is emerging as a crucial node in autophagy induction. However, the regulation of ULK1 is not fully understood. In this study, we identified TOPK (T-LAK cell-originated protein kinase), an oncokinase, as a novel upstream kinase to phosphorylate ULK1. We found that TOPK could directly bind with and phosphorylate ULK1 at Ser469, Ser495, and Ser533. The phosphorylation of ULK1 at Ser469, Ser495, and Ser533 by TOPK decreased the activity and stability ...[more]